MSH3_HUMAN - dbPTM
MSH3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSH3_HUMAN
UniProt AC P20585
Protein Name DNA mismatch repair protein Msh3
Gene Name MSH3
Organism Homo sapiens (Human).
Sequence Length 1137
Subcellular Localization
Protein Description Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis..
Protein Sequence MSRRKPASGGLAASSSAPARQAVLSRFFQSTGSLKSTSSSTGAADQVDPGAAAAAAAAAAAAPPAPPAPAFPPQLPPHIATEIDRRKKRPLENDGPVKKKVKKVQQKEGGSDLGMSGNSEPKKCLRTRNVSKSLEKLKEFCCDSALPQSRVQTESLQERFAVLPKCTDFDDISLLHAKNAVSSEDSKRQINQKDTTLFDLSQFGSSNTSHENLQKTASKSANKRSKSIYTPLELQYIEMKQQHKDAVLCVECGYKYRFFGEDAEIAARELNIYCHLDHNFMTASIPTHRLFVHVRRLVAKGYKVGVVKQTETAALKAIGDNRSSLFSRKLTALYTKSTLIGEDVNPLIKLDDAVNVDEIMTDTSTSYLLCISENKENVRDKKKGNIFIGIVGVQPATGEVVFDSFQDSASRSELETRMSSLQPVELLLPSALSEQTEALIHRATSVSVQDDRIRVERMDNIYFEYSHAFQAVTEFYAKDTVDIKGSQIISGIVNLEKPVICSLAAIIKYLKEFNLEKMLSKPENFKQLSSKMEFMTINGTTLRNLEILQNQTDMKTKGSLLWVLDHTKTSFGRRKLKKWVTQPLLKLREINARLDAVSEVLHSESSVFGQIENHLRKLPDIERGLCSIYHKKCSTQEFFLIVKTLYHLKSEFQAIIPAVNSHIQSDLLRTVILEIPELLSPVEHYLKILNEQAAKVGDKTELFKDLSDFPLIKKRKDEIQGVIDEIRMHLQEIRKILKNPSAQYVTVSGQEFMIEIKNSAVSCIPTDWVKVGSTKAVSRFHSPFIVENYRHLNQLREQLVLDCSAEWLDFLEKFSEHYHSLCKAVHHLATVDCIFSLAKVAKQGDYCRPTVQEERKIVIKNGRHPVIDVLLGEQDQYVPNNTDLSEDSERVMIITGPNMGGKSSYIKQVALITIMAQIGSYVPAEEATIGIVDGIFTRMGAADNIYKGQSTFMEELTDTAEIIRKATSQSLVILDELGRGTSTHDGIAIAYATLEYFIRDVKSLTLFVTHYPPVCELEKNYSHQVGNYHMGFLVSEDESKLDPGAAEQVPDFVTFLYQITRGIAARSYGLNVAKLADVPGEILKKAAHKSKELEGLINTKRKRLKYFAKLWTMHNAQDLQKWTEEFNMEETQTSLLH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
8PhosphorylationMSRRKPASGGLAASS
CCCCCCCCCCCCCCC		41.7524719451
14PhosphorylationASGGLAASSSAPARQ
CCCCCCCCCCHHHHH		21.1519664995
15PhosphorylationSGGLAASSSAPARQA
CCCCCCCCCHHHHHH		26.2821406692
16PhosphorylationGGLAASSSAPARQAV
CCCCCCCCHHHHHHH		35.4621406692
30PhosphorylationVLSRFFQSTGSLKST
HHHHHHHHCCCCCCC		29.5828450419
31PhosphorylationLSRFFQSTGSLKSTS
HHHHHHHCCCCCCCC		21.7328450419
33PhosphorylationRFFQSTGSLKSTSSS
HHHHHCCCCCCCCCC		32.4823401153
102UbiquitinationGPVKKKVKKVQQKEG
CCCHHHHHHHHHCCC		56.9922817900
103UbiquitinationPVKKKVKKVQQKEGG
CCHHHHHHHHHCCCC		48.5422817900
103AcetylationPVKKKVKKVQQKEGG
CCHHHHHHHHHCCCC		48.5420167786
107UbiquitinationKVKKVQQKEGGSDLG
HHHHHHHCCCCCCCC		41.0322817900
111PhosphorylationVQQKEGGSDLGMSGN
HHHCCCCCCCCCCCC		40.2821815630
116PhosphorylationGGSDLGMSGNSEPKK
CCCCCCCCCCCCCHH		32.7820068231
119PhosphorylationDLGMSGNSEPKKCLR
CCCCCCCCCCHHHHH		59.8221815630
138AcetylationSKSLEKLKEFCCDSA
HHHHHHHHHHHCCCC		60.8726051181
165UbiquitinationERFAVLPKCTDFDDI
HHHCCCCCCCCCCHH		45.6829967540
166GlutathionylationRFAVLPKCTDFDDIS
HHCCCCCCCCCCHHH		4.1022555962
178UbiquitinationDISLLHAKNAVSSED
HHHHHHHHHCCCCHH		34.3929967540
193UbiquitinationSKRQINQKDTTLFDL
HHHHHCCCCCCEEHH		53.1829967540
201PhosphorylationDTTLFDLSQFGSSNT
CCCEEHHHHHCCCCC		25.8817525332
208PhosphorylationSQFGSSNTSHENLQK
HHHCCCCCCHHHHHH		33.1521712546
209PhosphorylationQFGSSNTSHENLQKT
HHCCCCCCHHHHHHH		32.8121712546
215UbiquitinationTSHENLQKTASKSAN
CCHHHHHHHHHHHCC		49.5829967540
220PhosphorylationLQKTASKSANKRSKS
HHHHHHHHCCHHCCC		34.2822210691
225PhosphorylationSKSANKRSKSIYTPL
HHHCCHHCCCCCCHH		32.1522210691
227PhosphorylationSANKRSKSIYTPLEL
HCCHHCCCCCCHHHH		23.2929116813
229PhosphorylationNKRSKSIYTPLELQY
CHHCCCCCCHHHHHH		14.9229116813
230PhosphorylationKRSKSIYTPLELQYI
HHCCCCCCHHHHHHH		21.5229116813
236PhosphorylationYTPLELQYIEMKQQH
CCHHHHHHHHHHHHC		16.0929116813
240UbiquitinationELQYIEMKQQHKDAV
HHHHHHHHHHCCCCE		33.7329967540
244UbiquitinationIEMKQQHKDAVLCVE
HHHHHHCCCCEEEEE		42.94-
254PhosphorylationVLCVECGYKYRFFGE
EEEEECCCEEEECCC		19.2629978859
255AcetylationLCVECGYKYRFFGED
EEEECCCEEEECCCC		18.4226051181
308UbiquitinationGYKVGVVKQTETAAL
CCCEEEEECCCHHHH		49.4429967540
310PhosphorylationKVGVVKQTETAALKA
CEEEEECCCHHHHHH		29.5922985185
316MethylationQTETAALKAIGDNRS
CCCHHHHHHHCCCHH		32.9882981177
316UbiquitinationQTETAALKAIGDNRS
CCCHHHHHHHCCCHH		32.9829967540
337PhosphorylationLTALYTKSTLIGEDV
HHHHHCCCCCCCCCC		22.20-
338PhosphorylationTALYTKSTLIGEDVN
HHHHCCCCCCCCCCC		24.7720886841
520PhosphorylationFNLEKMLSKPENFKQ
CCHHHHHCCCHHHHH		42.5429449344
540PhosphorylationEFMTINGTTLRNLEI
EEEEECCCCHHCHHH		20.40-
541PhosphorylationFMTINGTTLRNLEIL
EEEECCCCHHCHHHH		25.72-
557SumoylationNQTDMKTKGSLLWVL
CCCCCCCCCCEEHHH		40.77-
557UbiquitinationNQTDMKTKGSLLWVL
CCCCCCCCCCEEHHH		40.77-
557SumoylationNQTDMKTKGSLLWVL
CCCCCCCCCCEEHHH		40.77-
586UbiquitinationWVTQPLLKLREINAR
HHHHHHHHHHHHHHH		53.86-
695UbiquitinationILNEQAAKVGDKTEL
HHHHHHHHHCCCHHH		50.1729967540
704UbiquitinationGDKTELFKDLSDFPL
CCCHHHHHCHHCCCH		71.0829967540
713UbiquitinationLSDFPLIKKRKDEIQ
HHCCCHHHCCHHHHH		54.9629967540
770UbiquitinationCIPTDWVKVGSTKAV
ECCCCCEEECCCHHH		36.3029967540
775UbiquitinationWVKVGSTKAVSRFHS
CEEECCCHHHHCCCC		48.7925015289
839AcetylationDCIFSLAKVAKQGDY
HHHHHHHHHHHCCCC		48.2826051181
842UbiquitinationFSLAKVAKQGDYCRP
HHHHHHHHCCCCCCC		58.7729967540
860UbiquitinationEERKIVIKNGRHPVI
CCCEEEECCCCCCCE		42.3227667366
902UbiquitinationTGPNMGGKSSYIKQV
ECCCCCCCHHHHHHH		30.42-
921PhosphorylationIMAQIGSYVPAEEAT
HHHHHCCCCCHHHCC		12.7725954137
937PhosphorylationGIVDGIFTRMGAADN
EEECCHHHHCCCCCC		20.1625954137
967PhosphorylationAEIIRKATSQSLVIL
HHHHHHHHCCCEEEE		30.27-
968PhosphorylationEIIRKATSQSLVILD
HHHHHHHCCCEEEEE		23.72-
1054PhosphorylationEQVPDFVTFLYQITR
HHCCHHHHHHHHHHH		14.12-
1068PhosphorylationRGIAARSYGLNVAKL
HHHHHHHCCCCHHHH		21.7817053785
1074UbiquitinationSYGLNVAKLADVPGE
HCCCCHHHHCCCCHH		39.67-
1085UbiquitinationVPGEILKKAAHKSKE
CCHHHHHHHHHHCHH		47.57-
1091UbiquitinationKKAAHKSKELEGLIN
HHHHHHCHHHHHHHH		71.7429967540
1099PhosphorylationELEGLINTKRKRLKY
HHHHHHHHHHHHHHH		25.8220068231
1100UbiquitinationLEGLINTKRKRLKYF
HHHHHHHHHHHHHHH		51.9729967540
11002-HydroxyisobutyrylationLEGLINTKRKRLKYF
HHHHHHHHHHHHHHH		51.97-
1105AcetylationNTKRKRLKYFAKLWT
HHHHHHHHHHHHHHH		42.2126051181
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MSH3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSH3_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MSH3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_HUMANPCNAphysical
11274057
PCNA_HUMANPCNAphysical
11005803
MSH2_HUMANMSH2physical
10029069
XPA_HUMANXPAphysical
19468048
RFA4_HUMANRPA4physical
19468048
MSH6_HUMANMSH6physical
22939629
OTU7B_HUMANOTUD7Bphysical
22939629
ORAV1_HUMANORAOV1physical
22939629
RFA1_HUMANRPA1physical
22939629
ZN363_HUMANRCHY1physical
21988832
PCNA_HUMANPCNAphysical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608089Endometrial cancer (ENDMC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MSH3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1068, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory